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dc.contributor.author
Vitturi, Dario A.
dc.contributor.author
Chen, Chen Shan
dc.contributor.author
Woodcock, Steven R.
dc.contributor.author
Salvatore, Sonia R.
dc.contributor.author
Bonacci, Gustavo Roberto
dc.contributor.author
Koenitzer, Jeffrey R.
dc.contributor.author
Stewart, Nicolas A.
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Wakabayashi, Nobunao
dc.contributor.author
Kensler, Thomas W.
dc.contributor.author
Freeman, Bruce A.
dc.contributor.author
Schopfer, Francisco J.
dc.date.available
2017-10-05T21:24:15Z
dc.date.issued
2013-08
dc.identifier.citation
Vitturi, Dario A.; Chen, Chen Shan; Woodcock, Steven R.; Salvatore, Sonia R.; Bonacci, Gustavo Roberto; et al.; Modulation of Nitro-fatty acid signaling: prostaglandin reductase-1 is a Nitroalkene reductase; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 288; 35; 8-2013; 25626-25637
dc.identifier.issn
0021-9258
dc.identifier.uri
http://hdl.handle.net/11336/26046
dc.description.abstract
Background: Nitroalkenes are electrophilic anti-inflammatory mediators that signal via Michael addition and are metabolized in vivo. Results: Prostaglandin reductase-1 is identified as a nitroalkene reductase. Conclusion: Prostaglandin reductase-1 reduces fatty acid nitroalkenes to nitroalkanes, inactivating electrophilic reactivity. Significance: A mammalian enzyme is identified that metabolizes fatty acid nitroalkenes in vivo to silence their signaling reactions.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
American Society for Biochemistry and Molecular Biology
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
dc.subject
Eicosanoid-Specific Enzymes
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Electrophile
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Nitro-Fatty Acid
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Redox Signaling
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Bioquímica y Biología Molecular
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Ciencias Biológicas
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CIENCIAS NATURALES Y EXACTAS
dc.title
Modulation of Nitro-fatty acid signaling: prostaglandin reductase-1 is a Nitroalkene reductase
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2017-10-02T19:05:09Z
dc.journal.volume
288
dc.journal.number
35
dc.journal.pagination
25626-25637
dc.journal.pais
Estados Unidos
dc.description.fil
Fil: Vitturi, Dario A.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Chen, Chen Shan. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Woodcock, Steven R.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Salvatore, Sonia R.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Bonacci, Gustavo Roberto. University of Pittsburgh; Estados Unidos. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
dc.description.fil
Fil: Koenitzer, Jeffrey R.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Stewart, Nicolas A.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Wakabayashi, Nobunao. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Kensler, Thomas W.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Freeman, Bruce A.. University of Pittsburgh; Estados Unidos
dc.description.fil
Fil: Schopfer, Francisco J.. University of Pittsburgh; Estados Unidos
dc.journal.title
Journal of Biological Chemistry (online)
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.1074/jbc.M113.486282
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/http://www.jbc.org/content/288/35/25626
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3757223/
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